Product Pathways - Protein Stability
PSMG1/PAC1 Antibody #13378
|13378S||100 µl (10 western blots)||---||In Stock||---|
|13378||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
PSMG1/PAC1 Antibody recognizes endogenous levels of total PSMG1 (PAC1) protein in human and monkey cells. This antibody weakly cross-reacts with murine and rat PSMG1 (PAC1) protein. This antibody does not cross-react with PSMG2 (PAC2) protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human PSMG1 (PAC1) protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from various cell lines using PSMG1/PAC1 Antibody.
Immunoprecipitation of PSMG1 from 293T cell extracts using Normal Rabbit IgG #2729 (lane 2) or PSMG1/PAC1 Antibody (lane 3). Lane 1 is 10% input. Western blot analysis was performed using PSMG1/PAC1 Antibody.
Western blot analysis of extracts from 293T cells, mock transfected (-) or transfected with constructs expressing Myc/DDK-tagged full-length human PSMG1 protein (hPSMG1-Myc/DDK; +) or Myc/DDK-tagged full-length human PSMG2 protein (hPSMG2-Myc/DDK; +), using PSMG1/PAC1 Antibody (upper) and DYKDDDDK Tag Antibody #2368 (lower).
The 26S proteasome is a highly abundant, ~2 MDa complex that serves as the proteolytic arm of the ubiquitin-proteasome system. It consists largely of two sub-complexes, the 19S regulatory particle (RP) and the 20S catalytic core particle (CP); in many cases two RPs cap either end of a CP. The CP is made of two stacked β-rings that contain the catalytic sites, each of which is made of seven subunits (β1-7), flanked on either side by two α-rings, which are also made of seven subunits each (α1-7). Thus, the structure of the 20S CP is α1-7β1-7β1-7α1-7. The RP includes a base and a lid. The base, in part, is composed of a hexametric ring of ATPases that function to unfold the substrate and open the gate of the interlacing amino-terminal segments of the α-subunits, thus allowing entry of the unfolded substrate into the catalytic chamber. The lid is predominantly involved in specific recognition of the ubiquitin signal (1). In addition to the 19S cap, other proteins and complexes, such as proteasome activator 28 (PA28/11S), bind to the end of the 20S cylinder and activate it by facilitating opening of the gate. Furthermore, proteasome-associated DUBs and E3s can remodel substrate-anchored polyubiquitin chains, which may modulate their susceptibility to degradation (2).
Proteasome assembly chaperone 1 (PSMG1, PAC1) is an evolutionarily conserved, ubiquitously expressed chaperone protein that promotes proper biogenesis of the α-ring of the 20S CP of the eukaryotic proteasome (3,4). PSMG1 (PAC1) functions in a heterodimeric complex with PSMG2 (PAC2) and was originally identified as a proteasome subunit binding partner (4). Intact PSMG1-PSMG2 heterodimers both promote heteroheptameric α-ring assembly and/or stability and prevent accumulation of non-productive α-ring dimers (4). Research studies targeting the disruption of the murine Psmg1 locus have substantiated the importance of proteasome chaperones in contributing to normal proteasome maturation and cellular homeostasis by demonstrating that loss of Psmg1/Pac1 function leads to embryonic lethality (5).
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